› 2lqg

Solution NMR

Solution Structure of the R4 domain of talin

Released:
DOI: 10.2210/pdb2lqg/pdb
PDB entry 2lqg coloured by chain, ensemble of 20 models, front view.
PDB entry 2lqg coloured by chain, ensemble of 20 models, side view.
PDB entry 2lqg coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover.
Goult BT, Zacharchenko T, Bate N, Tsang R, Hey F, Gingras AR, Elliott PR, Roberts GCK, Ballestrem C, Critchley DR, Barsukov IL
J Biol Chem 288 8238-8249 (2013)
PMID: 23389036

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150641 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Talin-1 Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 13.92 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26039 (Residues: 913-1044; Coverage: 5%)
Gene names: Tln, Tln1
Sequence domains: Talin, R4 domain
Structure domains: Alpha-catenin/vinculin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 95%
Refinement method: simulated annealing, molecular dynamics, torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

33 review citations

Talins and kindlins: partners in integrin-mediated adhesion.
Calderwood et al. (2013)
32 more

4 mentions without citation

RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover.
Goult et al. (2013)
3 more